Recombinant Mouse Heat shock protein 105 kDa (Hsph1), partial

Code CSB-YP713984MO
MSDS
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Source Yeast
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Code CSB-EP713984MO
MSDS
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Source E.coli
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Code CSB-EP713984MO-B
MSDS
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP713984MO
MSDS
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Source Baculovirus
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Code CSB-MP713984MO
MSDS
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
Uniprot No.
Alternative Names
Hsph1; Hsp105; Hsp110; Kiaa0201Heat shock protein 105 kDa; 42 degrees C-HSP; Heat shock 110 kDa protein; Heat shock-related 100 kDa protein E7I; HSP-E7I
Species
Mus musculus (Mouse)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Acts as a nucleotide-exchange factor (NEF) for chaperone proteins HSPA1A and HSPA1B, promoting the release of ADP from HSPA1A/B thereby triggering client/substrate protein release. Prevents the aggregation of denatured proteins in cells under severe stress, on which the ATP levels decrease markedly. Inhibits HSPA8/HSC70 ATPase and chaperone activities.
Gene References into Functions
  1. Hsp105 may play an important role in the refolding of denatured proteins and protection against stress-induced cell death in mammalian cells. PMID: 21557931
  2. Hsp110 over-expression increases the immunogenicity of the murine CT26 colon tumor. PMID: 12111119
  3. Data suggest that Hsp105 has opposite effects on stress-induced apoptosis depending on the cell type; a pro-apoptotic effect in embryonal cells and an anti-apoptotic effect in neuronal cells. PMID: 12153726
  4. enhances activation of p38, release of cytochrome c and caspase activation; may play important roles in organogenesis, during which marked apoptosis occurs, by enhancing apoptosis during mouse embryogenesis PMID: 12180991
  5. Hsp105alpha is suggested to regulate the substrate binding cycle of Hsp70/Hsc70 by inhibiting the ATPase activity of Hsp70/Hsc70, thereby functioning as a negative regulator of the Hsp70/Hsc70 chaperone system. PMID: 15292236
  6. The constitutive overexpression of HSP105 in cancer cells is involved in malignant transformation by protecting tumor cells from apoptosis. PMID: 16827803
  7. it is suggested that Hsp105 suppresses the stress-induced apoptosis at its initial step, the translocation of Bax to mitochondria PMID: 16857185
  8. hsp110/105 KO mice are resistant to ischemic injury and that the protective effects of hsp110/105 deficiency in cerebral ischemia may partly be mediated by an increase in the chaperone activity of Hsp70. PMID: 18658041

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Subcellular Location
Cytoplasm. Nucleus. Note=Strictly cytoplasmic in neurons.
Protein Families
Heat shock protein 70 family
Tissue Specificity
Highly expressed in testis. Present at lower levels in most brain regions, except cerebellum. Within the brain, expression is restricted to neurons (at protein level). Overexpressed in cancer cells.
Database Links
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301-363-4651 (Available 9 a.m. to 5 p.m. CST from Monday to Friday)
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Address
7505 Fannin St., Ste 610, Room 7 (CUBIO Innovation Center), Houston, TX 77054, USA
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